PSME4

PSME4
Identifiers
Aliases	PSME4, PA200, proteasome activator subunit 4
External IDs	OMIM: 607705; MGI: 2143994; HomoloGene: 113742; GeneCards: PSME4; OMA:PSME4 - orthologs
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2p16.2 Start 53,864,069 bp[1] End 53,970,993 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 A4 Start 30,721,726 bp[2] End 30,830,361 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sperm glutes gastrocnemius muscle left testis biceps brachii right testis Skeletal muscle tissue of biceps brachii deltoid muscle triceps brachii muscle vastus lateralis muscle Top expressed in temporal muscle triceps brachii muscle vastus lateralis muscle sternocleidomastoid muscle digastric muscle myocardium of ventricle gastrocnemius muscle spermatid medial head of gastrocnemius muscle cardiac muscles More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding peptidase activator activity lysine-acetylated histone binding proteasome binding Cellular component cytoplasm nuclear speck proteasome complex nucleus nucleoplasm cytosol proteasome core complex spermatoproteasome complex Biological process cell differentiation regulation of cellular amino acid metabolic process antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent regulation of mRNA stability positive regulation of canonical Wnt signaling pathway protein polyubiquitination stimulatory C-type lectin receptor signaling pathway tumor necrosis factor-mediated signaling pathway MAPK cascade cellular response to DNA damage stimulus positive regulation of peptidase activity multicellular organism development Fc-epsilon receptor signaling pathway NIK/NF-kappaB signaling spermatogenesis anaphase-promoting complex-dependent catabolic process T cell receptor signaling pathway negative regulation of canonical Wnt signaling pathway DNA repair proteasome-mediated ubiquitin-dependent protein catabolic process Wnt signaling pathway, planar cell polarity pathway proteasomal ubiquitin-independent protein catabolic process negative regulation of G2/M transition of mitotic cell cycle protein deubiquitination SCF-dependent proteasomal ubiquitin-dependent protein catabolic process transmembrane transport regulation of transcription from RNA polymerase II promoter in response to hypoxia post-translational protein modification regulation of hematopoietic stem cell differentiation interleukin-1-mediated signaling pathway regulation of mitotic cell cycle phase transition Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23198 103554 Ensembl ENSG00000068878 ENSMUSG00000040850 UniProt Q14997 Q5SSW2 RefSeq (mRNA) NM_014614 NM_134013 RefSeq (protein) NP_055429 NP_598774 Location (UCSC) Chr 2: 53.86 – 53.97 Mb Chr 11: 30.72 – 30.83 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Proteasome activator complex subunit 4 is a protein that in humans is encoded by the PSME4 gene.^[5][6][7]

References

1. GRCh38: Ensembl release 89: ENSG00000068878 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000040850 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S (Dec 1995). "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1". DNA Research. 1 (5): 223–9. doi:10.1093/dnares/1.5.223. PMID 7584044.
6. Ustrell V, Hoffman L, Pratt G, Rechsteiner M (Jul 2002). "PA200, a nuclear proteasome activator involved in DNA repair". The EMBO Journal. 21 (13): 3516–25. doi:10.1093/emboj/cdf333. PMC 126083. PMID 12093752.
7. "Entrez Gene: PSME4 proteasome (prosome, macropain) activator subunit 4".

Further reading

• Goff SP (Aug 2003). "Death by deamination: a novel host restriction system for HIV-1". Cell. 114 (3): 281–3. doi:10.1016/S0092-8674(03)00602-0. PMID 12914693. S2CID 16340355.
• Seeger M, Ferrell K, Frank R, Dubiel W (Mar 1997). "HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation". The Journal of Biological Chemistry. 272 (13): 8145–8. doi:10.1074/jbc.272.13.8145. PMID 9079628.
• Madani N, Kabat D (Dec 1998). "An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein". Journal of Virology. 72 (12): 10251–5. doi:10.1128/JVI.72.12.10251-10255.1998. PMC 110608. PMID 9811770.
• Simon JH, Gaddis NC, Fouchier RA, Malim MH (Dec 1998). "Evidence for a newly discovered cellular anti-HIV-1 phenotype". Nature Medicine. 4 (12): 1397–400. doi:10.1038/3987. PMID 9846577. S2CID 25235070.
• Mulder LC, Muesing MA (Sep 2000). "Degradation of HIV-1 integrase by the N-end rule pathway". The Journal of Biological Chemistry. 275 (38): 29749–53. doi:10.1074/jbc.M004670200. PMID 10893419.
• Sheehy AM, Gaddis NC, Choi JD, Malim MH (Aug 2002). "Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein". Nature. 418 (6898): 646–50. Bibcode:2002Natur.418..646S. doi:10.1038/nature00939. PMID 12167863. S2CID 4403228.
• Huang X, Seifert U, Salzmann U, Henklein P, Preissner R, Henke W, Sijts AJ, Kloetzel PM, Dubiel W (Nov 2002). "The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing". Journal of Molecular Biology. 323 (4): 771–82. doi:10.1016/S0022-2836(02)00998-1. PMID 12419264.
• Gaddis NC, Chertova E, Sheehy AM, Henderson LE, Malim MH (May 2003). "Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions". Journal of Virology. 77 (10): 5810–20. doi:10.1128/JVI.77.10.5810-5820.2003. PMC 154025. PMID 12719574.
• Lecossier D, Bouchonnet F, Clavel F, Hance AJ (May 2003). "Hypermutation of HIV-1 DNA in the absence of the Vif protein". Science. 300 (5622): 1112. doi:10.1126/science.1083338. PMID 12750511. S2CID 20591673.
• Zhang H, Yang B, Pomerantz RJ, Zhang C, Arunachalam SC, Gao L (Jul 2003). "The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA". Nature. 424 (6944): 94–8. Bibcode:2003Natur.424...94Z. doi:10.1038/nature01707. PMC 1350966. PMID 12808465.
• Mangeat B, Turelli P, Caron G, Friedli M, Perrin L, Trono D (Jul 2003). "Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts". Nature. 424 (6944): 99–103. Bibcode:2003Natur.424...99M. doi:10.1038/nature01709. PMID 12808466. S2CID 4347374.
• Harris RS, Bishop KN, Sheehy AM, Craig HM, Petersen-Mahrt SK, Watt IN, Neuberger MS, Malim MH (Jun 2003). "DNA deamination mediates innate immunity to retroviral infection". Cell. 113 (6): 803–9. doi:10.1016/S0092-8674(03)00423-9. PMID 12809610. S2CID 544971.
• Harris RS, Sheehy AM, Craig HM, Malim MH, Neuberger MS (Jul 2003). "DNA deamination: not just a trigger for antibody diversification but also a mechanism for defense against retroviruses". Nature Immunology. 4 (7): 641–3. doi:10.1038/ni0703-641. PMID 12830140. S2CID 5549252.
• Gu Y, Sundquist WI (Jul 2003). "Good to CU". Nature. 424 (6944): 21–2. Bibcode:2003Natur.424...21G. doi:10.1038/424021a. PMID 12840737. S2CID 4430569.
• Mariani R, Chen D, Schröfelbauer B, Navarro F, König R, Bollman B, Münk C, Nymark-McMahon H, Landau NR (Jul 2003). "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif". Cell. 114 (1): 21–31. doi:10.1016/S0092-8674(03)00515-4. PMID 12859895. S2CID 1789911.
• KewalRamani VN, Coffin JM (Aug 2003). "Virology. Weapons of mutational destruction". Science. 301 (5635): 923–5. doi:10.1126/science.1088965. PMID 12920286. S2CID 82480782.